Stability of the endo-beta-1,4-glucanase and beta-1,4-glucosidase from Bacteroides succinogenes.
The endo-beta-1,4-glucanase (carboxymethylcellulase) activity in cell extracts prepared from Bacteroides succinogenes S85 was almost unaffected by prolonged incubation at 39 degrees C in the presence of merthiolate, a sulfhydryl inhibitor. The beta-1,4-glucosidase (cellobiase) activity, however, was rapidly inactivated by the same treatment. The cellobiase was also inactivated by exposure to air, but was stabilized by dithiothreitol in a nitrogen atmosphere. These results suggest that the cellobiase required reduced sulfhydryl groups for activity.
D001439:Bacteroides / Q000201:enzymology*; D002480:Cellulase / Q000378:metabolism*; D004229:Dithiothreitol / Q000494:pharmacology; D005959:Glucosidases / Q000378:metabolism*; D006358:Hot Temperature; D010100:Oxygen / Q000494:pharmacology; D013439:Sulfhydryl Reagents / Q000494:pharmacology; D013849:Thimerosal / Q000494:pharmacology; D001617:beta-Glucosidase / Q000378:metabolism*
D013439:Sulfhydryl Reagents; D013849:Thimerosal; D005959:Glucosidases; D001617:beta-Glucosidase; D002480:Cellulase; D010100:Oxygen; D004229:Dithiothreitol